与细胞色素分子界面S100A8 b558和NADPH氧化酶激活。
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Berthier年代,阮MV, Baillet Hograindleur MA Paclet MH,波兰人B,莫雷尔F
与细胞色素分子界面S100A8 b558和NADPH氧化酶激活。
《公共科学图书馆•综合》。2012;7 (7):e40277。doi: 10.1371 / journal.pone.0040277。Epub 2012 7月10。
- PubMed ID
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22808130 (在PubMed]
- 文摘
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S100A8和S100A9是两个绑定骨髓相关的蛋白质,钙和炎性疾病的重要介质。他们最近推出了作为合作伙伴吞噬细胞NADPH氧化酶的监管。然而,他们相互作用的确切机制仍然是难以捉摸的。我们对目标(i)评估S100蛋白NADPH氧化酶活动的影响;(2)要么S100A8描述分子间相互作用,S100A9,或S100A8 / S100A9 heterocomplex细胞色素b (558);和(3)确定S100A8共识网站参与细胞色素b (558) / S100接口。重组完整长度或S100A9-A8截断嵌合体蛋白质和ExoS-S100融合蛋白分别表示在大肠杆菌和绿脓杆菌。我们的结果表明,S100A8功能性伙伴NADPH氧化酶激活S100A9相反,然而,装运和钙结合磷酸化S100A9体内至关重要。内源性S100A9和S100A8 colocalize分化和PMA刺激PLB985细胞,与Nox2 / gp91 (phox)和第22位(phox)。重组S100A8,富含钙和融合与第一129和54 n端氨基酸残基的铜绿假单胞菌外毒素,引起类似的氧化酶激活体外,与所观察到的S100A8 S100A9体内的存在。 This suggests that S100A8 is the essential component of the S100A9/S100A8 heterocomplex for oxidase activation. In this context, recombinant full-length rS100A9-A8 and rS100A9-A8 truncated 90 chimera proteins as opposed to rS100A9-A8 truncated 86 and rS100A9-A8 truncated 57 chimeras, activate the NADPH oxidase function of purified cytochrome b(558) suggesting that the C-terminal region of S100A8 is directly involved in the molecular interface with the hemoprotein. The data point to four strategic (87)HEES(90) amino acid residues of the S100A8 C-terminal sequence that are involved directly in the molecular interaction with cytochrome b(558) and then in the phagocyte NADPH oxidase activation.